ID   ASNS1_YEAST             Reviewed;         572 AA.
AC   P49089; D6W4E2;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 200.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 1;
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase 1;
GN   Name=ASN1; OrderedLocusNames=YPR145W; ORFNames=P9659.3;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8951815; DOI=10.1046/j.1365-2958.1996.d01-1715.x;
RA   Dang V.D., Valens M., Bolotin-Fukuhara M., Daignan-Fornier B.;
RT   "Cloning of the ASN1 and ASN2 genes encoding asparagine synthetases in
RT   Saccharomyces cerevisiae: differential regulation by the CCAAT-box-binding
RT   factor.";
RL   Mol. Microbiol. 22:681-692(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875; DOI=10.1038/387s103;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-509, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate + L-glutamine + ATP + H2O = L-asparagine + L-
CC         glutamate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:12228,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.4;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC       asparagine from L-aspartate (L-Gln route): step 1/1.
CC   -!- INTERACTION:
CC       P49089; P49090: ASN2; NbExp=2; IntAct=EBI-3043, EBI-3048;
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DR   EMBL; Z48675; CAA88594.1; -; Genomic_DNA.
DR   EMBL; U40829; AAB68284.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11558.1; -; Genomic_DNA.
DR   PIR; S52694; S52694.
DR   RefSeq; NP_015471.1; NM_001184242.1.
DR   AlphaFoldDB; P49089; -.
DR   SMR; P49089; -.
DR   BioGRID; 36314; 88.
DR   DIP; DIP-3810N; -.
DR   FunCoup; P49089; 705.
DR   IntAct; P49089; 8.
DR   STRING; 4932.YPR145W; -.
DR   iPTMnet; P49089; -.
DR   PaxDb; 4932-YPR145W; -.
DR   PeptideAtlas; P49089; -.
DR   EnsemblFungi; YPR145W_mRNA; YPR145W; YPR145W.
DR   GeneID; 856268; -.
DR   KEGG; sce:YPR145W; -.
DR   AGR; SGD:S000006349; -.
DR   SGD; S000006349; ASN1.
DR   VEuPathDB; FungiDB:YPR145W; -.
DR   eggNOG; KOG0571; Eukaryota.
DR   HOGENOM; CLU_014658_2_2_1; -.
DR   InParanoid; P49089; -.
DR   OMA; HYLNFHA; -.
DR   OrthoDB; 409189at2759; -.
DR   BioCyc; YEAST:YPR145W-MONOMER; -.
DR   Reactome; R-SCE-8963693; Aspartate and asparagine metabolism.
DR   UniPathway; UPA00134; UER00195.
DR   BioGRID-ORCS; 856268; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P49089; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P49089; protein.
DR   GO; GO:0097268; C:cytoophidium; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IDA:SGD.
DR   GO; GO:0070981; P:L-asparagine biosynthetic process; IGI:SGD.
DR   CDD; cd01991; Asn_synthase_B_C; 1.
DR   CDD; cd00712; AsnB; 1.
DR   FunFam; 3.40.50.620:FF:000031; Asparagine synthase B; 1.
DR   FunFam; 3.60.20.10:FF:000050; Asparagine synthetase 2; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR006426; Asn_synth_AEB.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR050795; Asn_Synthetase.
DR   InterPro; IPR033738; AsnB_N.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR01536; asn_synth_AEB; 1.
DR   NCBIfam; NF006949; PRK09431.1; 1.
DR   PANTHER; PTHR11772; ASPARAGINE SYNTHETASE; 1.
DR   PANTHER; PTHR11772:SF2; ASPARAGINE SYNTHETASE [GLUTAMINE-HYDROLYZING]; 1.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding;
KW   Glutamine amidotransferase; Ligase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..572
FT                   /note="Asparagine synthetase [glutamine-hydrolyzing] 1"
FT                   /id="PRO_0000056917"
FT   DOMAIN          2..186
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          194..546
FT                   /note="Asparagine synthetase"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         49..53
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250"
FT   BINDING         74..76
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         366..367
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            368
FT                   /note="Important for beta-aspartyl-AMP intermediate
FT                   formation"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         509
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   572 AA;  64470 MW;  39F2873F0E689FC9 CRC64;
     MCGIFAAFRH EDVHRYKPKA LQLSKRIRHR GPDWSGNAIK NSTIFVHERL AIVGVESGAQ
     PITSSDGEYM LCVNGEIYNH IQLREECADY EFGTLSDCEP IIPMYLKHDI DAPKYLDGMF
     AWTLYDAKQD RIVAARDPIG ITTLYMGRSS ASPKTVYFAS ELKCLTDDCD TITAFPPGHV
     YDSKTDKITR YFTPDWLDEK RIPSTPIDYM AIRHSLEKAV RKRLMAEVPY GVLLSGGLDS
     SLIASIAARE TAKATNDVEP STYDSKARHL AGIDDDGKLH TAGWTSLHSF AIGLPNAPDL
     QAARKVAKFI GSIHHEHTFT LQEGLDALDD VIYHLETYDV TTIRASTPMF LLSRKIKAQG
     VKMVLSGEGS DEIFGGYLYF AQAPSAAEFH TESVQRVKNL HLADCLRANK STMAWGLEAR
     VPFLDREFLQ LCMNIDPNEK MIKPKEGRIE KYILRKAFDT TGEPDAKPYL PEEILWRQKE
     QFSDGVGYSW IDGLKDTAEA VISDEMFASP KAEWGSDIPT TKEAFWYRLK FDALFPQKTV
     ADTVMRWIPK ADWGCAEDPS GRYAQIHEKH IE
//